ID GST2_CAEEL Reviewed; 188 AA.
AC O16115; Q21356;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Glutathione S-transferase 2;
DE EC=2.5.1.18;
DE AltName: Full=CeGST2;
DE AltName: Full=GST class-sigma;
GN Name=gst-2; ORFNames=K08F4.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RA Tawe W.N., Eschbach M.-L., Walter R.D., Henkle-Duehrsen K.;
RT "Paraquat mediates differential gene expression in C. elegans.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000250|UniProtKB:P46436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000250|UniProtKB:P46436};
CC -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC {ECO:0000305}.
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DR EMBL; AF010240; AAB65418.1; -; mRNA.
DR EMBL; Z68879; CAA93087.2; -; Genomic_DNA.
DR PIR; T23484; T23484.
DR PIR; T37463; T37463.
DR RefSeq; NP_501847.1; NM_069446.3.
DR AlphaFoldDB; O16115; -.
DR SMR; O16115; -.
DR STRING; 6239.K08F4.6.1; -.
DR PaxDb; 6239-K08F4-6; -.
DR EnsemblMetazoa; K08F4.6.1; K08F4.6.1; WBGene00001750.
DR EnsemblMetazoa; K08F4.6.2; K08F4.6.2; WBGene00001750.
DR GeneID; 177884; -.
DR KEGG; cel:CELE_K08F4.6; -.
DR UCSC; K08F4.6; c. elegans.
DR AGR; WB:WBGene00001750; -.
DR WormBase; K08F4.6; CE25051; WBGene00001750; gst-2.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00970000196017; -.
DR HOGENOM; CLU_039475_1_0_1; -.
DR InParanoid; O16115; -.
DR OMA; YDFRWLT; -.
DR OrthoDB; 1385810at2759; -.
DR PhylomeDB; O16115; -.
DR PRO; PR:O16115; -.
DR Proteomes; UP000001940; Chromosome IV.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR CDD; cd03192; GST_C_Sigma_like; 1.
DR CDD; cd03039; GST_N_Sigma_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF44; GLUTATHIONE S-TRANSFERASE 2-RELATED; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Transferase.
FT CHAIN 1..188
FT /note="Glutathione S-transferase 2"
FT /id="PRO_0000185925"
FT DOMAIN 2..79
FT /note="GST N-terminal"
FT DOMAIN 81..188
FT /note="GST C-terminal"
FT BINDING 43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P46088"
FT BINDING 49..51
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 63..64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
SQ SEQUENCE 188 AA; 21848 MW; 06B095CC022C7CED CRC64;
MVHYKLMCFD VRGLGEVIRQ LFYLGDVSFE DFRVSREEFK SLKSNLPSGQ LPVLEIDGVM
ISQSASIGRF LARQYGYSGK TPTEEMQVDS IIDLFKDFML TFRQFFFAVI HGYPEYEKER
MKRDIVKPAI KNYFIALNKI LLRSKSGFLV GDDLTWADLQ IADNLSTLIN IRLFAEKEPH
LNVFIRKL
//
